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Yorodumi- PDB-2flg: Solution structure of an EGF-LIKE domain from the Plasmodium falc... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2flg | ||||||
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Title | Solution structure of an EGF-LIKE domain from the Plasmodium falciparum merozoite surface protein 1 | ||||||
Components | Merozoite surface protein 1 | ||||||
Keywords | SURFACE ACTIVE PROTEIN / EGF-LIKE DOMAIN / EXTRACELLULAR / MODULAR PROTEIN / SURFACE ANTIGEN / MALARIA VACCINE COMPONENT / SURFACE PROTEIN | ||||||
Function / homology | Function and homology information vacuolar membrane / side of membrane / extracellular region / plasma membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | James, S. / Moehle, K. / Pluschke, G. / Robinson, J. | ||||||
Citation | Journal: Chembiochem / Year: 2006 Title: Synthesis, solution structure and immune recognition of an epidermal growth factor-like domain from Plasmodium falciparum merozoite surface protein-1. Authors: James, S. / Moehle, K. / Renard, A. / Mueller, M.S. / Vogel, D. / Zurbriggen, R. / Pluschke, G. / Robinson, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2flg.cif.gz | 298.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2flg.ent.gz | 248 KB | Display | PDB format |
PDBx/mmJSON format | 2flg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2flg_validation.pdf.gz | 344.6 KB | Display | wwPDB validaton report |
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Full document | 2flg_full_validation.pdf.gz | 447.8 KB | Display | |
Data in XML | 2flg_validation.xml.gz | 14.4 KB | Display | |
Data in CIF | 2flg_validation.cif.gz | 23.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fl/2flg ftp://data.pdbj.org/pub/pdb/validation_reports/fl/2flg | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 5600.310 Da / Num. of mol.: 1 / Fragment: C-TERMINAL FRAGMENT, residues 1526-1573 / Source method: obtained synthetically Details: The protein occurs naturally in Plasmodium falciparum References: UniProt: P04933 |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.25 MM FIRST N-TERMINAL EGF-LIKE DOMAIN of MSP1(19), 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0 mM / pH: 5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS AND LOWEST TARGET FUNCTION Conformers calculated total number: 100 / Conformers submitted total number: 20 |